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Treadmilling analysis reveals new insights into dynamic FtsZ ring architecture

MPS-Authors
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Ramirez-Diaz,  Diego A.
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Garcia-Soriano,  Daniela
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Raso,  Ana
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Mücksch,  Jonas
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Schwille,  Petra
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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journal.pbio.2004845.pdf
(Publisher version), 9MB

Supplementary Material (public)

6288593.zip
(Supplementary material), 19MB

Citation

Ramirez-Diaz, D. A., Garcia-Soriano, D., Raso, A., Mücksch, J., Feingold, M., Rivas, G., et al. (2018). Treadmilling analysis reveals new insights into dynamic FtsZ ring architecture. PLoS Biology, 16(5): e2004845. doi:10.1371/journal.pbio.2004845.


Cite as: https://hdl.handle.net/21.11116/0000-0003-C3C3-4
Abstract
FtsZ, the primary protein of the bacterial Z ring guiding cell division, has been recently shown to engage in intriguing treadmilling dynamics along the circumference of the division plane. When coreconstituted in vitro with FtsA, one of its natural membrane anchors, on flat supported membranes, these proteins assemble into dynamic chiral vortices compatible with treadmilling of curved polar filaments. Replacing FtsA by a membrane-targeting sequence (mts) to FtsZ, we have discovered conditions for the formation of dynamic rings, showing that the phenomenon is intrinsic to FtsZ. Ring formation is only observed for a narrow range of protein concentrations at the bilayer, which is highly modulated by free Mg2+ and depends upon guanosine triphosphate (GTP) hydrolysis. Interestingly, the direction of rotation can be reversed by switching the mts from the C-terminus to the N-terminus of the protein, implying that the filament attachment must have a perpendicular component to both curvature and polarity. Remarkably, this chirality switch concurs with previously shown inward or outward membrane deformations by the respective FtsZ mutants. Our results lead us to suggest an intrinsic helicity of FtsZ filaments with more than one direction of curvature, supporting earlier hypotheses and experimental evidence.